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Calmodulin-dependent protein phosphorylation in synaptic junctions.

P T Kelly, R K Yip, S M Shields

    Journal of Neurochemistry
    |November 1, 1985
    PubMed
    Summary
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    Synaptic junctions (SJs) concentrate Ca2+/calmodulin (CaM)-dependent kinase activity, phosphorylating key proteins. This suggests Ca2+/CaM-dependent protein phosphorylation plays a vital role in synaptic communication mechanisms.

    Area of Science:

    • Neuroscience
    • Molecular Biology
    • Biochemistry

    Background:

    • Synaptic junctions (SJs) are critical for neuronal communication.
    • Calcium/calmodulin (Ca2+/CaM) signaling is essential for synaptic plasticity and function.
    • Understanding the enzymatic machinery at SJs is key to deciphering synaptic transmission.

    Purpose of the Study:

    • To investigate the presence and activity of Ca2+/calmodulin (CaM)-dependent kinase in rat forebrain synaptic junctions (SJs).
    • To compare the kinase activity in SJs with synaptic plasma membrane (SPM) and postsynaptic density (PSD) fractions.
    • To identify endogenous substrates phosphorylated by Ca2+/CaM-dependent kinase in SJs.

    Main Methods:

    • Isolation of synaptic junction (SJ), synaptic plasma membrane (SPM), and postsynaptic density (PSD) fractions from rat forebrain.

    Related Experiment Videos

  • Assay of Ca2+/calmodulin (CaM)-dependent kinase activity by measuring endogenous protein phosphorylation and exogenous synapsin I phosphorylation.
  • Identification and characterization of phosphorylated proteins using molecular weight and binding properties.

    • Main Results:

    • Synaptic junctions (SJs) exhibited significantly higher Ca2+/calmodulin (CaM)-dependent kinase activity compared to SPM and PSD fractions.
    • Ca2+/CaM strongly stimulated the phosphorylation of specific SJ proteins, including 60- and 50-kDa polypeptides (major PSD protein).
    • Several other proteins, including synapsin I, were identified as substrates for CaM-dependent kinase in SJs, with phosphorylation occurring at serine and/or threonine residues.

    Conclusions:

    • Brain synaptic junctions (SJs) are enriched with Ca2+/calmodulin (CaM)-dependent kinase and its substrate proteins.
    • CaM-dependent protein phosphorylation at SJs likely plays a crucial role in synaptic communication.
    • The dynamic equilibrium of SJ-associated CaM suggests its regulation by cytoplasmic factors.